Naslov
Screening for glucose-triggered modifications of glutathione

Autori
Jerić, Ivanka ; Horvat, Štefica

Izvornik
Journal of peptide science (1075-2617) 15 (2009), 8; 540-547

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
glutathione ; glycation ; Amadori ; thiazolidine ; mass spectrometry ; Maillard

Sažetak
Nonenzymatic protein glycation is caused by a Schiff's base reaction between the aldehyde groups of reducing sugars and the primary amines of proteins. These structures may undergo further Amadori rearrangement and free radical-mediated oxidation to finally generate irreversible advanced glycation end products (AGEs). One of the factors known to modulate the glycation of proteins is glutathione, the most abundant nonprotein thiol tripeptide with the  -linkage, H-Glu(Cys-Gly-OH)-OH (GSH). Screening for products formed by GSH with D-glucose is an essential step in understanding the participation of GSH in glycation (the Maillard) reaction. Under the conditions used in these studies we observed N-(1-deoxy-D-fructos-1-yl)-pyroglutamic acid as the major glycation product formed in the mixtures of GSH and glucose in vitro. A reversed-phase HPLC/MS and tandem mass spectrometry analyses of the GSH/glucose mixtures revealed that cleavage of the N-terminal glutamic acid and the formation of pyroglutamic acid-related Amadori product was accompanied by Cys-Gly-derived Amadori and thiazolidine compounds.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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